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[NMR paper] Unraveling motion in proteins by combining NMR relaxometry and molecular dynamics simulations: A case study on ubiquitin
Mar 11, 2024 - 10:30 PM - by nmrlearner
nmrlearner's Avatar Unraveling motion in proteins by combining NMR relaxometry and molecular dynamics simulations: A case study on ubiquitin

Nuclear magnetic resonance (NMR) relaxation experiments shine light onto the dynamics of molecular systems in the picosecond to millisecond timescales. As these methods cannot provide an atomically resolved view of the motion of atoms, functional groups, or domains giving rise to such signals, relaxation techniques have been combined with molecular dynamics (MD) simulations to obtain mechanistic descriptions and gain insights into the functional role of side chain or domain motion. In this work,...

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0 Replies | 57 Views
[NMR paper] Sedimentation of large, soluble proteins up to 140 kDa for 1H-detected MAS NMR and 13C DNP NMR - practical aspects
Mar 11, 2024 - 10:30 PM - by nmrlearner
nmrlearner's Avatar Sedimentation of large, soluble proteins up to 140 kDa for 1H-detected MAS NMR and 13C DNP NMR - practical aspects

Solution NMR is typically applied to biological systems with molecular weights < 40 kDa whereas magic-angle-spinning (MAS) solid-state NMR traditionally targets very large, oligomeric proteins and complexes exceeding 500 kDa in mass, including fibrils and crystalline protein preparations. Here, we propose that the gap between these size regimes can be filled by the approach presented that enables investigation of large, soluble and fully protonated proteins in the range of 40-140 kDa. As a key...

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0 Replies | 38 Views
Solid-state NMR MAS CryoProbe enables structural studies of human blood protein vitronectin bound to hydroxyapatite - ScienceDirect.com
Mar 11, 2024 - 4:18 AM - by nmrlearner
nmrlearner's Avatar Solid-state NMR MAS CryoProbe enables structural studies of human blood protein vitronectin bound to hydroxyapatite - ScienceDirect.com

Solid-state NMR MAS CryoProbe enables structural studies of human blood protein vitronectin bound to hydroxyapatite ScienceDirect.com Read here
0 Replies | 40 Views
NMR solution structure determination of large RNA-protein complexes - ScienceDirect.com
Mar 11, 2024 - 4:18 AM - by nmrlearner
nmrlearner's Avatar NMR solution structure determination of large RNA-protein complexes - ScienceDirect.com

NMR solution structure determination of large RNA-protein complexes ScienceDirect.com Read here
0 Replies | 57 Views
[NMR paper] Genetically encoded site-specific (19)F unnatural amino acid incorporation in V. natriegens for in-cell NMR analysis
Mar 11, 2024 - 4:18 AM - by nmrlearner
nmrlearner's Avatar Genetically encoded site-specific (19)F unnatural amino acid incorporation in V. natriegens for in-cell NMR analysis

Nuclear magnetic resonance (NMR) spectroscopy NMR is a well-established technique for probing protein structure, dynamics and conformational changes. Taking advantage of the high signal sensitivity and broad chemical shift range of ^(19)F nuclei, ^(19)F NMR has been applied to investigate protein function at atomic resolution. In this report, we extend the unnatural amino acid site-specific incorporation into V. natriegens, an alternate protein expression system. The unnatural amino acid...

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0 Replies | 97 Views
[NMR paper] NMR study of the structure and dynamics of the BRCT domain from the kinetochore protein KKT4
Mar 09, 2024 - 12:05 AM - by nmrlearner
nmrlearner's Avatar NMR study of the structure and dynamics of the BRCT domain from the kinetochore protein KKT4

KKT4 is a multi-domain kinetochore protein specific to kinetoplastids, such as Trypanosoma brucei. It lacks significant sequence similarity to known kinetochore proteins in other eukaryotes. Our recent X-ray structure of the C-terminal region of KKT4 shows that it has a tandem BRCT (BRCA1 C Terminus) domain fold with a sulfate ion bound in a typical binding site for a phosphorylated serine or threonine. Here we present the ¹H, ^(13)C and ^(15)N resonance assignments for the BRCT domain of KKT4...

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0 Replies | 231 Views
[NMR paper] High-efficiency low-power (13)C-(15)N cross polarization in MAS NMR
Mar 09, 2024 - 12:05 AM - by nmrlearner
nmrlearner's Avatar High-efficiency low-power (13)C-(15)N cross polarization in MAS NMR

Biomolecular solid-state magic angle spinning (MAS) NMR spectroscopy frequently relies on selective ^(13)C-^(15)N magnetization transfers, for various kinds of correlation experiments. Introduced in 1998, spectrally induced filtering in combination with cross polarization (SPECIFIC-CP) is a selective heteronuclear magnetization transfer experiment widely used for biological applications. At MAS frequencies below 20 kHz, commonly used for ^(13)C-detected MAS NMR experiments, SPECIFIC-CP transfer...

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0 Replies | 42 Views
Atomic resolution conformational dynamics of intrinsically disordered proteins from NMR spin relaxation - ScienceDirect.com
Mar 07, 2024 - 10:30 PM - by nmrlearner
nmrlearner's Avatar Atomic resolution conformational dynamics of intrinsically disordered proteins from NMR spin relaxation - ScienceDirect.com

Atomic resolution conformational dynamics of intrinsically disordered proteins from NMR spin relaxation ScienceDirect.com Read here
0 Replies | 63 Views
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